[1] Rodriguez-Morales AJ, Castañeda-Hernández DM. Bacteria: Mycobacterium bovis. Encyclopedia of Food Safety. 2014: 468-475. DOI:http://dx.doi.org/10.1016/B978-0-12-378612-8.00103-7.
[2] Moda G, Daborn CJ, Grange JM, Cosivi O. The zoonotic importance of Mycobacterium bovis. Tubercle and Lung Disease. 1996;77(2):103-8. https://doi.org/10.1016/S0962-8479(96)90022-2.
[3] Organization WH. Report of the WHO Meeting on Zoonotic Tuberculosis (Mycobacterium bovis, Geneva, 15 November 1993. World Health Organization; 1993. DOI: https://doi.org/10.1016/s0962-8479(96)90022-2.
[4] Hoft DF, Gheorghiu M. Mucosal immunity induced by oral administration of bacille Calmette–Guérin. Mucosal vaccines, Elsevier; 1996, p. 269–79. DOI: https://doi.org/10.1016/B978-012410580-5/50021-2.
[5] Meije Y, Martínez-Montauti J, Caylà JA, Loureiro J, Ortega L, Clemente M, et al. Healthcare-Associated Mycobacterium bovis–Bacille Calmette-Guérin (BCG) Infection in Cancer Patients Without Prior BCG Instillation. Clinical Infectious Diseases. 2017;65(7):1136-43. https://doi.org/10.1093/cid/cix496.
[6] Nimrod G, Schushan M, Steinberg DM, Ben-Tal N. Detection of functionally important regions in “hypothetical proteins” of known structure. Structure. 2008;16(12):1755-63. https://doi.org/10.1016/j.str.2008.10.017.
[7] Chaudhry GR, Chapalamadugu S. Biodegradation of halogenated organic compounds. Microbiological reviews. 1991;55(1):59-79. https://doi.org/10.1128/mr.55.1.59-79.1991.
[8] Furukawa K, Simon JR, Chakrabarty AM. Common induction and regulation of biphenyl, xylene/toluene, and salicylate catabolism in Pseudomonas paucimobilis. Journal of Bacteriology. 1983;154(3):1356-62. https://doi.org/10.1128/jb.154.3.1356-1362.1983.
[9] Margesin R, Labbe D, Schinner F, Greer CW, Whyte LG. Characterization of hydrocarbon-degrading microbial populations in contaminated and pristine alpine soils. Applied and Environmental Microbiology. 2003;69(6):3085-92. https://doi.org/10.1128/AEM.69.6.3085-3092.2003.
[10] Kovalcik A, Obruca S, Fritz I, Marova I. Polyhydroxyalkanoates: their importance and future. BioResources. 2019;14(2):2468-71.
[11] Steinbüchel A. Recent advances in the knowledge of the metabolism of bacterial polyhydroxyalkanoic acids and potential impacts on the production of biodegradable thermoplastics. Acta biotechnologica. 1991;11(5):419-27. https://doi.org/10.1002/abio.370110504.
[12]Muhammadi, Shabina, Afzal M, Hameed S. Bacterial polyhydroxyalkanoates-eco-friendly next generation plastic: production, biocompatibility, biodegradation, physical properties and applications. Green Chemistry Letters and Reviews. 2015;8(3-4):56-77. https://doi.org/10.1080/17518253.2015.1109715.
[13] Zinn M, Witholt B, Egli T. Occurrence, synthesis and medical application of bacterial polyhydroxyalkanoate. Advanced drug delivery reviews. 2001;53(1):5-21. https://doi.org/10.1016/S0169-409X(01)00218-6.
[14] Steinbüchel A, Lütke-Eversloh T. Metabolic engineering and pathway construction for biotechnological production of relevant polyhydroxyalkanoates in microorganisms. Biochemical engineering journal. 2003;16(2):81-96. https://doi.org/10.1016/S1369-703X(03)00036-6.
[15] Koller M, Maršálek L, de Sousa Dias MM, Braunegg G. Producing microbial polyhydroxyalkanoate (PHA) biopolyesters in a sustainable manner. New biotechnology. 2017;37:24-38. https://doi.org/10.1016/j.nbt.2016.05.001.
[16] Gasteiger E, Gattiker A, Hoogland C, Ivanyi I, Appel RD, Bairoch A. ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res 2003;31:3784–8. DOI: https://doi.org/10.1093/nar/gkg563.
[17] Guruprasad K, Reddy BB, Pandit MW. Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence. Protein Engineering, Design and Selection. 1990;4(2):155-61. https://doi.org/10.1093/protein/4.2.155.
[18] Barh D, Tiwari S, Jain N, Ali A, Santos AR, Misra AN, et al. In silico subtractive genomics for target identification in human bacterial pathogens. Drug Development Research. 2011;72(2):162-77. https://doi.org/10.1002/ddr.20413.
[19] Yu CS, Chen YC, Lu CH, Hwang JK. Prediction of protein subcellular localization. Proteins: Structure, Function, and Bioinformatics. 2006;64(3):643-51. https://doi.org/10.1002/prot.21018.
[20] Yu NY, Wagner JR, Laird MR, Melli G, Rey S, Lo R, et al. PSORTb 3.0: improved protein subcellular localization prediction with refined localization subcategories and predictive capabilities for all prokaryotes. Bioinformatics. 2010;26(13):1608-15. https://doi.org/10.1093/bioinformatics/btq249.
[21] Bhasin M, Garg A, Raghava GP. PSLpred: prediction of subcellular localization of bacterial proteins. Bioinformatics. 2005;21(10):2522-4. https://doi.org/10.1093/bioinformatics/bti309.
[22] Imai K, Asakawa N, Tsuji T, Akazawa F, Ino A, Sonoyama M, et al. SOSUI-GramN: high performance prediction for sub-cellular localization of proteins in gram-negative bacteria. Bioinformation. 2008;2(9):417. doi: 10.6026/97320630002417.
[23] Möller S, Croning MD, Apweiler R. Evaluation of methods for the prediction of membrane spanning regions. Bioinformatics. 2001;17(7):646-53. https://doi.org/10.1093/bioinformatics/17.7.646.
[24] Tusnady GE, Simon I. The HMMTOP transmembrane topology prediction server. Bioinformatics. 2001;17(9):849-50. https://doi.org/10.1093/bioinformatics/17.9.849.
[25] Dobson L, Reményi I, Tusnády GE. CCTOP: a Consensus Constrained TOPology prediction web server. Nucleic acids research. 2015;43(W1):W408-12. https://doi.org/10.1093/nar/gkv451.
[26] von Heijne PT. G. et al SignalP 4.0: discriminating signal peptides from transmembrane regions. Nat. Methods.2011;8:785-6. DOI: https://doi.org/10.1038/nmeth.1701.
[27] Bendtsen JD, Kiemer L, Fausbøll A, Brunak S. Non-classical protein secretion in bacteria. BMC microbiology. 2005;5(1):1-3. https://doi.org/10.1186/1471-2180-5-58.
[28] Boeckmann B, Bairoch A, Apweiler R. Blatter 2. MC, Estreicher A, Gasteiger E, Martin MJ, Michoud K, O’Donovan C, Phan I, Pilbout S, Schneider M (2003) The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003. Nucleic Acids Res.;31:365-70. DOI: https://doi.org/10.1093/nar/gkg095.
[29] Finn RD, Bateman A, Clements J. Co ggill P., Eberhardt RY, Eddy SR et al. Pfam: the protein families database. Nucleic Acids Res 2014;42:D222–30. DOI: https://doi.org/10.1093/nar/gkt1223.
[30] Wilson D, Madera M, Vogel C, Chothia C, Gough J. The SUPERFAMILY database in 2007: families and functions. Nucleic Acids Res 2007;35:D308–13. DOI: https://doi.org/10.1093/nar/gkl910.
[31] Lupas A, Van Dyke M, Stock J. Predicting coiled coils from protein sequences. Science. 1991:1162-4.
[32] Hunter S, Apweiler R, Attwood TK, Bairoch A, Bateman A, Binns D, et al. InterPro: the integrative protein signature database. Nucleic acids research. 2009;37(suppl_1):D211-5. https://doi.org/10.1093/nar/gkn785.
[33] Shen HB, Chou KC. Predicting protein fold pattern with functional domain and sequential evolution information. Journal of Theoretical Biology. 2009;256(3):441-6. https://doi.org/10.1016/j.jtbi.2008.10.007.
[36] Kokkinidis M, Glykos NM, Fadouloglou VE. Protein flexibility and enzymatic catalysis. Advances in protein chemistry and structural biology. 2012;87:181-218. https://doi.org/10.1016/B978-0-12-398312-1.00007-X.
[37] Neill SD, Pollock JM, Bryson DB, Hanna J. Pathogenesis of Mycobacterium bovis infection in cattle. Veterinary microbiology. 1994;40(1-2):41-52. https://doi.org/10.1016/0378-1135(94)90045-0.
[38] Hooda V, babu Gundala P, Chinthala P. Sequence analysis and homology modeling of peroxidase from Medicago sativa. Bioinformation. 2012;8(20):974-979. doi: 10.6026/97320630008974.
[39] Fukui T, Shiomi N, Doi Y. Expression and characterization of (R)-specific enoyl coenzyme A hydratase involved in polyhydroxyalkanoate biosynthesis by Aeromonas caviae. Journal of Bacteriology. 1998;180(3):667-73.
https://doi.org/10.1128/JB.180.3.667-673.1998.